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Database: UniProt
Entry: A0A0E3UMS9_9GAMM
LinkDB: A0A0E3UMS9_9GAMM
Original site: A0A0E3UMS9_9GAMM 
ID   A0A0E3UMS9_9GAMM        Unreviewed;       199 AA.
AC   A0A0E3UMS9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Cytochrome c-type protein {ECO:0000256|PIRNR:PIRNR000013};
GN   ORFNames=WQ53_05665 {ECO:0000313|EMBL:AKC86335.1};
OS   Pseudoxanthomonas suwonensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=314722 {ECO:0000313|EMBL:AKC86335.1, ECO:0000313|Proteomes:UP000033067};
RN   [1] {ECO:0000313|EMBL:AKC86335.1, ECO:0000313|Proteomes:UP000033067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J1 {ECO:0000313|EMBL:AKC86335.1,
RC   ECO:0000313|Proteomes:UP000033067};
RX   PubMed=26067962;
RA   Hou L., Jiang J., Xu Z., Zhou Y., Leung F.C.;
RT   "Complete Genome Sequence of Pseudoxanthomonas suwonensis Strain J1, a
RT   Cellulose-Degrading Bacterium Isolated from Leaf- and Wood-Enriched Soil.";
RL   Genome Announc. 3:e00614-15(2015).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000013-1};
CC       Note=Binds 4 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000013-
CC       1};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- PTM: Binds 4 heme groups per subunit. {ECO:0000256|PIRNR:PIRNR000013}.
CC   -!- SIMILARITY: Belongs to the NapC/NirT/NrfH family.
CC       {ECO:0000256|ARBA:ARBA00007395}.
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DR   EMBL; CP011144; AKC86335.1; -; Genomic_DNA.
DR   RefSeq; WP_052631166.1; NZ_CP011144.1.
DR   AlphaFoldDB; A0A0E3UMS9; -.
DR   KEGG; psuw:WQ53_05665; -.
DR   PATRIC; fig|314722.6.peg.1199; -.
DR   eggNOG; COG3005; Bacteria.
DR   OrthoDB; 9782159at2; -.
DR   Proteomes; UP000033067; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019333; P:denitrification pathway; IEA:InterPro.
DR   Gene3D; 1.10.3820.10; Di-heme elbow motif domain; 1.
DR   InterPro; IPR036280; Multihaem_cyt_sf.
DR   InterPro; IPR024717; NapC/NirT/NrfH.
DR   InterPro; IPR005126; NapC/NirT_cyt_c_N.
DR   InterPro; IPR038266; NapC/NirT_cytc_sf.
DR   InterPro; IPR011885; NO3Rdtase_cyt_c_NapC/NirT.
DR   NCBIfam; TIGR02161; napC_nirT; 1.
DR   PANTHER; PTHR30333; CYTOCHROME C-TYPE PROTEIN; 1.
DR   PANTHER; PTHR30333:SF1; CYTOCHROME C-TYPE PROTEIN NAPC; 1.
DR   Pfam; PF03264; Cytochrom_NNT; 1.
DR   PIRSF; PIRSF000013; 4_hem_cytochrm_NapC; 1.
DR   SUPFAM; SSF48695; Multiheme cytochromes; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|PIRNR:PIRNR000013};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000013};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000013};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000013};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033067};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000013}.
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..193
FT                   /note="NapC/NirT cytochrome c N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03264"
FT   BINDING         56
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         59
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         62
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-2"
FT   BINDING         86
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         89
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         90
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-2"
FT   BINDING         108
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-2"
FT   BINDING         146
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="3"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         149
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="3"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         150
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="3"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-2"
FT   BINDING         179
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="4"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         182
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="4"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         183
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="4"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-2"
FT   BINDING         188
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-2"
SQ   SEQUENCE   199 AA;  22766 MW;  74483B91F2CE43E0 CRC64;
     MWARTKRHAL GLWRTLRSPS RYYSLGFLTV AGFIAGVLFW GGFNTALEAT NTEKFCTSCH
     EMRDNVFEEL KGTIHYTNRS GVRATCPDCH VPHDWTDKIA RKMQASKEVW GKLFGTINTR
     EKFLDERLVL ATHEWSRLKA NDSLECRNCH DFDSMDLTRQ SPRAAQIHRL WLGTGERTCI
     DCHKGIAHQL PNMAGVPQG
//
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